Thermodynamic evaluation and modeling of proton and water exchange associated with benzamidine and berenil binding to beta-trypsin.

@article{Pereira2005ThermodynamicEA,
  title={Thermodynamic evaluation and modeling of proton and water exchange associated with benzamidine and berenil binding to beta-trypsin.},
  author={M{\'a}rcio Tadeu Pereira and J M Silva-Alves and Andrelly Martins-Jos{\'e} and Julio Cesar Dias Lopes and Marcelo M. Santoro},
  journal={Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas},
  year={2005},
  volume={38 11},
  pages={1593-601}
}
Serine-proteases are involved in vital processes in virtually all species. They are important targets for researchers studying the relationships between protein structure and activity, for the rational design of new pharmaceuticals. Trypsin was used as a model to assess a possible differential contribution of hydration water to the binding of two synthetic inhibitors. Thermodynamic parameters for the association of bovine beta-trypsin (homogeneous material, observed 23,294.4 +/- 0.2 Da… CONTINUE READING